Prolyl isomerase Pin1 enhances osteoblast differentiation through Runx2 regulation

Sung Ho Lee; You Hee Choi; Yeon Jin Kim; Hong Seok Choi; Chang Yeol Yeo; Kwang Youl Lee

doi:10.1016/j.febslet.2013.09.040

Prolyl isomerase Pin1 enhances osteoblast differentiation through Runx2 regulation

Sung Ho Lee, You Hee Choi, Yeon Jin Kim, Hong Seok Choi, Chang Yeol Yeo, Kwang Youl Lee

Department of Life Science

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Peptidyl-prolyl isomerase 1 (Pin1) is the only enzyme known to catalyze isomerization of the pSer/Thr-Pro peptide bond. Pin1 induces conformational change of substrates and subsequently regulates diverse cellular processes. However, its role in osteoblast differentiation is not well understood. Here we show that Pin1 enhances osteoblast differentiation. Pin1 interacts and affects the protein stability and transcriptional activity of an important osteogenic transcriptional factor Runx2. Our results indicate that this regulation is likely due to suppression of poly-ubiquitination-mediated proteasomal degradation of Runx2. Our current finding suggests that Pin1 is a novel regulator of osteoblast differentiation that acts through the regulation of Runx2 function.

Original language	English
Pages (from-to)	3640-3647
Number of pages	8
Journal	FEBS Letters
Volume	587
Issue number	22
DOIs	https://doi.org/10.1016/j.febslet.2013.09.040
State	Published - 15 Nov 2013

Bibliographical note

Funding Information:
This work is supported by the National Research Foundation of Korea (NRF) grants funded by the Korea government (MSIP) to C.-Y.Y. (No. 2012R1A5A1048236 ) and K.Y.L. ( 2011-0022259 ).

Keywords

Osteoblast differentiation
Pin1
Runx2

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title = "Prolyl isomerase Pin1 enhances osteoblast differentiation through Runx2 regulation",

abstract = "Peptidyl-prolyl isomerase 1 (Pin1) is the only enzyme known to catalyze isomerization of the pSer/Thr-Pro peptide bond. Pin1 induces conformational change of substrates and subsequently regulates diverse cellular processes. However, its role in osteoblast differentiation is not well understood. Here we show that Pin1 enhances osteoblast differentiation. Pin1 interacts and affects the protein stability and transcriptional activity of an important osteogenic transcriptional factor Runx2. Our results indicate that this regulation is likely due to suppression of poly-ubiquitination-mediated proteasomal degradation of Runx2. Our current finding suggests that Pin1 is a novel regulator of osteoblast differentiation that acts through the regulation of Runx2 function.",

keywords = "Osteoblast differentiation, Pin1, Runx2",

author = "Lee, {Sung Ho} and Choi, {You Hee} and Kim, {Yeon Jin} and Choi, {Hong Seok} and Yeo, {Chang Yeol} and Lee, {Kwang Youl}",

note = "Funding Information: This work is supported by the National Research Foundation of Korea (NRF) grants funded by the Korea government (MSIP) to C.-Y.Y. (No. 2012R1A5A1048236 ) and K.Y.L. ( 2011-0022259 ).",

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doi = "10.1016/j.febslet.2013.09.040",

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AU - Lee, Sung Ho

AU - Choi, You Hee

AU - Kim, Yeon Jin

AU - Choi, Hong Seok

AU - Yeo, Chang Yeol

AU - Lee, Kwang Youl

N1 - Funding Information: This work is supported by the National Research Foundation of Korea (NRF) grants funded by the Korea government (MSIP) to C.-Y.Y. (No. 2012R1A5A1048236 ) and K.Y.L. ( 2011-0022259 ).

PY - 2013/11/15

Y1 - 2013/11/15

N2 - Peptidyl-prolyl isomerase 1 (Pin1) is the only enzyme known to catalyze isomerization of the pSer/Thr-Pro peptide bond. Pin1 induces conformational change of substrates and subsequently regulates diverse cellular processes. However, its role in osteoblast differentiation is not well understood. Here we show that Pin1 enhances osteoblast differentiation. Pin1 interacts and affects the protein stability and transcriptional activity of an important osteogenic transcriptional factor Runx2. Our results indicate that this regulation is likely due to suppression of poly-ubiquitination-mediated proteasomal degradation of Runx2. Our current finding suggests that Pin1 is a novel regulator of osteoblast differentiation that acts through the regulation of Runx2 function.

AB - Peptidyl-prolyl isomerase 1 (Pin1) is the only enzyme known to catalyze isomerization of the pSer/Thr-Pro peptide bond. Pin1 induces conformational change of substrates and subsequently regulates diverse cellular processes. However, its role in osteoblast differentiation is not well understood. Here we show that Pin1 enhances osteoblast differentiation. Pin1 interacts and affects the protein stability and transcriptional activity of an important osteogenic transcriptional factor Runx2. Our results indicate that this regulation is likely due to suppression of poly-ubiquitination-mediated proteasomal degradation of Runx2. Our current finding suggests that Pin1 is a novel regulator of osteoblast differentiation that acts through the regulation of Runx2 function.

KW - Osteoblast differentiation

KW - Pin1

KW - Runx2

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U2 - 10.1016/j.febslet.2013.09.040

DO - 10.1016/j.febslet.2013.09.040

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AN - SCOPUS:84887407352

SN - 0014-5793

VL - 587

SP - 3640

EP - 3647

JO - FEBS Letters

JF - FEBS Letters

IS - 22

ER -

Prolyl isomerase Pin1 enhances osteoblast differentiation through Runx2 regulation

Abstract

Bibliographical note

Keywords

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